GB2336156A - Protein-based adhesive compositions - Google Patents
Protein-based adhesive compositions Download PDFInfo
- Publication number
- GB2336156A GB2336156A GB9807777A GB9807777A GB2336156A GB 2336156 A GB2336156 A GB 2336156A GB 9807777 A GB9807777 A GB 9807777A GB 9807777 A GB9807777 A GB 9807777A GB 2336156 A GB2336156 A GB 2336156A
- Authority
- GB
- United Kingdom
- Prior art keywords
- phenol
- composition
- adhesive
- protein
- oxidase
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Granted
Links
- 230000001070 adhesive effect Effects 0.000 title claims abstract description 61
- 239000000853 adhesive Substances 0.000 title claims abstract description 60
- 239000000203 mixture Substances 0.000 title claims abstract description 48
- 108090000623 proteins and genes Proteins 0.000 title claims description 38
- 102000004169 proteins and genes Human genes 0.000 title claims description 38
- 102000003425 Tyrosinase Human genes 0.000 claims abstract description 42
- 108060008724 Tyrosinase Proteins 0.000 claims abstract description 42
- 101710129170 Extensin Proteins 0.000 claims abstract description 37
- 108010027388 phenol 2-monooxygenase Proteins 0.000 claims abstract description 28
- 230000001588 bifunctional effect Effects 0.000 claims abstract description 25
- 239000003431 cross linking reagent Substances 0.000 claims abstract description 23
- 230000002255 enzymatic effect Effects 0.000 claims abstract description 20
- 235000001674 Agaricus brunnescens Nutrition 0.000 claims abstract description 11
- AZQWKYJCGOJGHM-UHFFFAOYSA-N 1,4-benzoquinone Chemical compound O=C1C=CC(=O)C=C1 AZQWKYJCGOJGHM-UHFFFAOYSA-N 0.000 claims abstract description 10
- YCIMNLLNPGFGHC-UHFFFAOYSA-N catechol Chemical compound OC1=CC=CC=C1O YCIMNLLNPGFGHC-UHFFFAOYSA-N 0.000 claims abstract description 6
- PFTAWBLQPZVEMU-DZGCQCFKSA-N (+)-catechin Chemical compound C1([C@H]2OC3=CC(O)=CC(O)=C3C[C@@H]2O)=CC=C(O)C(O)=C1 PFTAWBLQPZVEMU-DZGCQCFKSA-N 0.000 claims abstract description 3
- SXRSQZLOMIGNAQ-UHFFFAOYSA-N Glutaraldehyde Chemical compound O=CCCCC=O SXRSQZLOMIGNAQ-UHFFFAOYSA-N 0.000 claims abstract description 3
- ADRVNXBAWSRFAJ-UHFFFAOYSA-N catechin Natural products OC1Cc2cc(O)cc(O)c2OC1c3ccc(O)c(O)c3 ADRVNXBAWSRFAJ-UHFFFAOYSA-N 0.000 claims abstract description 3
- 235000005487 catechin Nutrition 0.000 claims abstract description 3
- 229950001002 cianidanol Drugs 0.000 claims abstract description 3
- 239000012948 isocyanate Substances 0.000 claims abstract description 3
- 238000000034 method Methods 0.000 claims description 27
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 20
- 239000000758 substrate Substances 0.000 claims description 19
- 238000004132 cross linking Methods 0.000 claims description 16
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N phenol group Chemical group C1(=CC=CC=C1)O ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 claims description 13
- 238000004519 manufacturing process Methods 0.000 claims description 9
- 239000002250 absorbent Substances 0.000 claims description 8
- 230000001939 inductive effect Effects 0.000 claims description 8
- 102000004316 Oxidoreductases Human genes 0.000 claims description 6
- 108090000854 Oxidoreductases Proteins 0.000 claims description 6
- 238000000576 coating method Methods 0.000 claims description 6
- 235000013824 polyphenols Nutrition 0.000 claims description 6
- QIGBRXMKCJKVMJ-UHFFFAOYSA-N Hydroquinone Chemical group OC1=CC=C(O)C=C1 QIGBRXMKCJKVMJ-UHFFFAOYSA-N 0.000 claims description 5
- 230000002745 absorbent Effects 0.000 claims description 4
- 239000011248 coating agent Substances 0.000 claims description 4
- -1 carpet Substances 0.000 claims description 3
- 229910052751 metal Inorganic materials 0.000 claims description 3
- 239000002184 metal Substances 0.000 claims description 3
- 229920000742 Cotton Polymers 0.000 claims description 2
- 239000003349 gelling agent Substances 0.000 claims description 2
- 239000003365 glass fiber Substances 0.000 claims description 2
- 239000010985 leather Substances 0.000 claims description 2
- 239000004033 plastic Substances 0.000 claims description 2
- 229920003023 plastic Polymers 0.000 claims description 2
- 239000004576 sand Substances 0.000 claims description 2
- 239000004753 textile Substances 0.000 claims description 2
- 239000002023 wood Substances 0.000 claims description 2
- 241000222519 Agaricus bisporus Species 0.000 claims 1
- 102000008109 Mixed Function Oxygenases Human genes 0.000 claims 1
- 108010074633 Mixed Function Oxygenases Proteins 0.000 claims 1
- 239000011230 binding agent Substances 0.000 claims 1
- 150000002085 enols Chemical class 0.000 claims 1
- NWONKYPBYAMBJT-UHFFFAOYSA-L zinc sulfate Chemical compound [Zn+2].[O-]S([O-])(=O)=O NWONKYPBYAMBJT-UHFFFAOYSA-L 0.000 claims 1
- 244000000626 Daucus carota Species 0.000 abstract description 10
- 235000002767 Daucus carota Nutrition 0.000 abstract description 10
- 241000196324 Embryophyta Species 0.000 abstract description 7
- 210000002421 cell wall Anatomy 0.000 abstract description 5
- 102000003886 Glycoproteins Human genes 0.000 abstract description 3
- 108090000288 Glycoproteins Proteins 0.000 abstract description 3
- 235000013305 food Nutrition 0.000 abstract description 2
- 238000002360 preparation method Methods 0.000 abstract description 2
- 239000004971 Cross linker Substances 0.000 abstract 2
- 239000008194 pharmaceutical composition Substances 0.000 abstract 1
- 235000018102 proteins Nutrition 0.000 description 33
- MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 16
- 102000003992 Peroxidases Human genes 0.000 description 10
- 230000003647 oxidation Effects 0.000 description 10
- 238000007254 oxidation reaction Methods 0.000 description 10
- WQGWDDDVZFFDIG-UHFFFAOYSA-N pyrogallol Chemical group OC1=CC=CC(O)=C1O WQGWDDDVZFFDIG-UHFFFAOYSA-N 0.000 description 10
- 241000237536 Mytilus edulis Species 0.000 description 9
- 235000020638 mussel Nutrition 0.000 description 9
- 125000003588 lysine group Chemical group [H]N([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 8
- 125000004151 quinonyl group Chemical group 0.000 description 8
- 230000008901 benefit Effects 0.000 description 6
- 125000001493 tyrosinyl group Chemical group [H]OC1=C([H])C([H])=C(C([H])=C1[H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 6
- 150000001413 amino acids Chemical class 0.000 description 5
- 230000015572 biosynthetic process Effects 0.000 description 5
- 230000033444 hydroxylation Effects 0.000 description 5
- 238000005805 hydroxylation reaction Methods 0.000 description 5
- 108040007629 peroxidase activity proteins Proteins 0.000 description 5
- 235000002374 tyrosine Nutrition 0.000 description 5
- 102000030523 Catechol oxidase Human genes 0.000 description 4
- 108010031396 Catechol oxidase Proteins 0.000 description 4
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 4
- 235000001014 amino acid Nutrition 0.000 description 4
- 238000006243 chemical reaction Methods 0.000 description 4
- 239000012153 distilled water Substances 0.000 description 4
- OQALFHMKVSJFRR-UHFFFAOYSA-N dityrosine Chemical compound OC(=O)C(N)CC1=CC=C(O)C(C=2C(=CC=C(CC(N)C(O)=O)C=2)O)=C1 OQALFHMKVSJFRR-UHFFFAOYSA-N 0.000 description 4
- 229960004441 tyrosine Drugs 0.000 description 4
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 4
- 108010010803 Gelatin Proteins 0.000 description 3
- PMMYEEVYMWASQN-DMTCNVIQSA-N Hydroxyproline Chemical compound O[C@H]1CN[C@H](C(O)=O)C1 PMMYEEVYMWASQN-DMTCNVIQSA-N 0.000 description 3
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 3
- 239000004472 Lysine Substances 0.000 description 3
- 108700020962 Peroxidase Proteins 0.000 description 3
- 238000007792 addition Methods 0.000 description 3
- 229940024606 amino acid Drugs 0.000 description 3
- 239000003795 chemical substances by application Substances 0.000 description 3
- VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 3
- PMMYEEVYMWASQN-UHFFFAOYSA-N dl-hydroxyproline Natural products OC1C[NH2+]C(C([O-])=O)C1 PMMYEEVYMWASQN-UHFFFAOYSA-N 0.000 description 3
- 230000000694 effects Effects 0.000 description 3
- 229920000159 gelatin Polymers 0.000 description 3
- 239000008273 gelatin Substances 0.000 description 3
- 235000019322 gelatine Nutrition 0.000 description 3
- 235000011852 gelatine desserts Nutrition 0.000 description 3
- 229960002591 hydroxyproline Drugs 0.000 description 3
- 238000002955 isolation Methods 0.000 description 3
- FGMPLJWBKKVCDB-UHFFFAOYSA-N trans-L-hydroxy-proline Natural products ON1CCCC1C(O)=O FGMPLJWBKKVCDB-UHFFFAOYSA-N 0.000 description 3
- CIWBSHSKHKDKBQ-JLAZNSOCSA-N Ascorbic acid Chemical compound OC[C@H](O)[C@H]1OC(=O)C(O)=C1O CIWBSHSKHKDKBQ-JLAZNSOCSA-N 0.000 description 2
- 229920001661 Chitosan Polymers 0.000 description 2
- WTDRDQBEARUVNC-LURJTMIESA-N L-DOPA Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C(O)=C1 WTDRDQBEARUVNC-LURJTMIESA-N 0.000 description 2
- 244000300264 Spinacia oleracea Species 0.000 description 2
- 235000009337 Spinacia oleracea Nutrition 0.000 description 2
- 239000007983 Tris buffer Substances 0.000 description 2
- 125000003118 aryl group Chemical group 0.000 description 2
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 2
- 239000000227 bioadhesive Substances 0.000 description 2
- 238000005341 cation exchange Methods 0.000 description 2
- 238000012512 characterization method Methods 0.000 description 2
- ZUOUZKKEUPVFJK-UHFFFAOYSA-N diphenyl Chemical compound C1=CC=CC=C1C1=CC=CC=C1 ZUOUZKKEUPVFJK-UHFFFAOYSA-N 0.000 description 2
- 239000001257 hydrogen Substances 0.000 description 2
- 229910052739 hydrogen Inorganic materials 0.000 description 2
- 230000001965 increasing effect Effects 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 230000007246 mechanism Effects 0.000 description 2
- 239000001301 oxygen Substances 0.000 description 2
- 229910052760 oxygen Inorganic materials 0.000 description 2
- 230000008569 process Effects 0.000 description 2
- 239000000243 solution Substances 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- FWZXNPNHUWFOCM-LSLKUGRBSA-N (2s)-2-amino-3-[4-[5-(2-amino-2-carboxyethyl)-2-hydroxyphenoxy]phenyl]propanoic acid Chemical compound C1=CC(C[C@H](N)C(O)=O)=CC=C1OC1=CC(CC(N)C(O)=O)=CC=C1O FWZXNPNHUWFOCM-LSLKUGRBSA-N 0.000 description 1
- WOAHJDHKFWSLKE-UHFFFAOYSA-N 1,2-benzoquinone Chemical compound O=C1C=CC=CC1=O WOAHJDHKFWSLKE-UHFFFAOYSA-N 0.000 description 1
- 150000005206 1,2-dihydroxybenzenes Chemical class 0.000 description 1
- HIXDQWDOVZUNNA-UHFFFAOYSA-N 2-(3,4-dimethoxyphenyl)-5-hydroxy-7-methoxychromen-4-one Chemical compound C=1C(OC)=CC(O)=C(C(C=2)=O)C=1OC=2C1=CC=C(OC)C(OC)=C1 HIXDQWDOVZUNNA-UHFFFAOYSA-N 0.000 description 1
- 101150034533 ATIC gene Proteins 0.000 description 1
- 244000251953 Agaricus brunnescens Species 0.000 description 1
- 101100277337 Arabidopsis thaliana DDM1 gene Proteins 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 1
- 102000016938 Catalase Human genes 0.000 description 1
- 108010053835 Catalase Proteins 0.000 description 1
- 108010037362 Extracellular Matrix Proteins Proteins 0.000 description 1
- 102000010834 Extracellular Matrix Proteins Human genes 0.000 description 1
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 1
- 241000257303 Hymenoptera Species 0.000 description 1
- YTQUPBPCMQTTSE-UHFFFAOYSA-N Isodityrosine Natural products NC(Cc1ccc(Oc2ccc(CC(N)C(=O)O)cc2O)cc1)C(=O)O YTQUPBPCMQTTSE-UHFFFAOYSA-N 0.000 description 1
- WTDRDQBEARUVNC-UHFFFAOYSA-N L-Dopa Natural products OC(=O)C(N)CC1=CC=C(O)C(O)=C1 WTDRDQBEARUVNC-UHFFFAOYSA-N 0.000 description 1
- 125000003798 L-tyrosyl group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C([H])([H])C1=C([H])C([H])=C(O[H])C([H])=C1[H] 0.000 description 1
- GQWNECFJGBQMBO-UHFFFAOYSA-N Molindone hydrochloride Chemical compound Cl.O=C1C=2C(CC)=C(C)NC=2CCC1CN1CCOCC1 GQWNECFJGBQMBO-UHFFFAOYSA-N 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 108010064851 Plant Proteins Proteins 0.000 description 1
- 239000004743 Polypropylene Substances 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 1
- 101150051432 SOM1 gene Proteins 0.000 description 1
- 229920002684 Sepharose Polymers 0.000 description 1
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 1
- 206010052428 Wound Diseases 0.000 description 1
- 208000027418 Wounds and injury Diseases 0.000 description 1
- 239000004480 active ingredient Substances 0.000 description 1
- 239000002998 adhesive polymer Substances 0.000 description 1
- 229960003767 alanine Drugs 0.000 description 1
- 125000003277 amino group Chemical group 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 150000001491 aromatic compounds Chemical class 0.000 description 1
- 229940072107 ascorbate Drugs 0.000 description 1
- 235000010323 ascorbic acid Nutrition 0.000 description 1
- 239000011668 ascorbic acid Substances 0.000 description 1
- 235000013405 beer Nutrition 0.000 description 1
- 239000004305 biphenyl Substances 0.000 description 1
- 235000010290 biphenyl Nutrition 0.000 description 1
- 238000006664 bond formation reaction Methods 0.000 description 1
- 239000007767 bonding agent Substances 0.000 description 1
- 239000001110 calcium chloride Substances 0.000 description 1
- 229910001628 calcium chloride Inorganic materials 0.000 description 1
- 150000001720 carbohydrates Chemical class 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 150000001768 cations Chemical class 0.000 description 1
- 210000004027 cell Anatomy 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 239000003638 chemical reducing agent Substances 0.000 description 1
- WIIZWVCIJKGZOK-RKDXNWHRSA-N chloramphenicol Chemical compound ClC(Cl)C(=O)N[C@H](CO)[C@H](O)C1=CC=C([N+]([O-])=O)C=C1 WIIZWVCIJKGZOK-RKDXNWHRSA-N 0.000 description 1
- 229960005091 chloramphenicol Drugs 0.000 description 1
- 239000002299 complementary DNA Substances 0.000 description 1
- 238000011109 contamination Methods 0.000 description 1
- 230000008878 coupling Effects 0.000 description 1
- 238000010168 coupling process Methods 0.000 description 1
- 238000005859 coupling reaction Methods 0.000 description 1
- JVXNCJLLOUQYBF-UHFFFAOYSA-N cyclohex-4-ene-1,3-dione Chemical compound O=C1CC=CC(=O)C1 JVXNCJLLOUQYBF-UHFFFAOYSA-N 0.000 description 1
- 238000012217 deletion Methods 0.000 description 1
- 230000037430 deletion Effects 0.000 description 1
- BZCOSCNPHJNQBP-OWOJBTEDSA-N dihydroxyfumaric acid Chemical compound OC(=O)C(\O)=C(/O)C(O)=O BZCOSCNPHJNQBP-OWOJBTEDSA-N 0.000 description 1
- 125000005442 diisocyanate group Chemical group 0.000 description 1
- 238000010828 elution Methods 0.000 description 1
- RTZKZFJDLAIYFH-UHFFFAOYSA-N ether Substances CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 1
- DNJIEGIFACGWOD-UHFFFAOYSA-N ethyl mercaptane Natural products CCS DNJIEGIFACGWOD-UHFFFAOYSA-N 0.000 description 1
- 239000011536 extraction buffer Substances 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- 125000004435 hydrogen atom Chemical class [H]* 0.000 description 1
- 230000003301 hydrolyzing effect Effects 0.000 description 1
- 125000004356 hydroxy functional group Chemical group O* 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- 238000011031 large-scale manufacturing process Methods 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 150000002739 metals Chemical class 0.000 description 1
- 239000012038 nucleophile Substances 0.000 description 1
- 230000001590 oxidative effect Effects 0.000 description 1
- 239000003973 paint Substances 0.000 description 1
- 239000013618 particulate matter Substances 0.000 description 1
- 230000001717 pathogenic effect Effects 0.000 description 1
- 239000008188 pellet Substances 0.000 description 1
- 150000002989 phenols Chemical class 0.000 description 1
- 239000008363 phosphate buffer Substances 0.000 description 1
- 235000021118 plant-derived protein Nutrition 0.000 description 1
- 229920001155 polypropylene Polymers 0.000 description 1
- 230000004481 post-translational protein modification Effects 0.000 description 1
- 108090000765 processed proteins & peptides Proteins 0.000 description 1
- 102000004196 processed proteins & peptides Human genes 0.000 description 1
- 239000011253 protective coating Substances 0.000 description 1
- 230000003252 repetitive effect Effects 0.000 description 1
- 239000001632 sodium acetate Substances 0.000 description 1
- 235000017281 sodium acetate Nutrition 0.000 description 1
- 239000011343 solid material Substances 0.000 description 1
- 238000006467 substitution reaction Methods 0.000 description 1
- 229920001187 thermosetting polymer Polymers 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- 229920002554 vinyl polymer Polymers 0.000 description 1
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 1
Classifications
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61L—METHODS OR APPARATUS FOR STERILISING MATERIALS OR OBJECTS IN GENERAL; DISINFECTION, STERILISATION OR DEODORISATION OF AIR; CHEMICAL ASPECTS OF BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES; MATERIALS FOR BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES
- A61L24/00—Surgical adhesives or cements; Adhesives for colostomy devices
- A61L24/04—Surgical adhesives or cements; Adhesives for colostomy devices containing macromolecular materials
- A61L24/10—Polypeptides; Proteins
- A61L24/106—Fibrin; Fibrinogen
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/415—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from plants
-
- C—CHEMISTRY; METALLURGY
- C09—DYES; PAINTS; POLISHES; NATURAL RESINS; ADHESIVES; COMPOSITIONS NOT OTHERWISE PROVIDED FOR; APPLICATIONS OF MATERIALS NOT OTHERWISE PROVIDED FOR
- C09J—ADHESIVES; NON-MECHANICAL ASPECTS OF ADHESIVE PROCESSES IN GENERAL; ADHESIVE PROCESSES NOT PROVIDED FOR ELSEWHERE; USE OF MATERIALS AS ADHESIVES
- C09J189/00—Adhesives based on proteins; Adhesives based on derivatives thereof
Abstract
An adhesive composition is described which comprises an extensin protein; either a non-enzymatic bifunctional cross-linking agent; or an enzymatic cross-linker comprising phenol oxidase and a phenol hydroxylase, preferably a mushroom tyrosinase. The extensin is a plant cell wall glycoprotein preferably prepared from carrots. The non-enzymatic bifunctional cross-linker is preferably a di-isocyanate, a quinone or glutaraldehyde. The composition preferably also comprises a co-factor such as catechol or catechin. The adhesive may be used in pharmaceutical compositions, in wound closing preparations, or as a gelling product in foods.
Description
1 - Adhesives The present invention relates 2336156 to water resistant
adhesives.
Adhesives are widely used both domestically and industrially. They are typically applied to dry first and second surfaces to bond the surfaces together,.,':or example as bonding agents to bond together particulate matter, or to adhere other solid materials such as woods and metals. it is often desired to bond surfaces together when one or more of the surfaces is wet. Many adhesives are, however, less effective or ineffective if the surfaces that are to be bonded together are wet or if water is applied to the bond after it has been formed. Consequently, much effort has been spent trying to identify and develop adhesives which are effective in wet environments.
Marine mussels are able to attach themselves to a variety of surfaces under water forming strong and durable bonds with those surfaces. The precise mechanism by which mussels achieve this adhesion is not known. J. H.Waite has described the proposed involvement of catechol oxidase and a phenolic protein (Mussel Beards: a coming of age. Chemistry & Industry, 1991, 607-611). The mussel polyphenolic protein is a highly repetitive protein which comprises 80 tandem repeats of a decapeptide of the sequence: Ala-Lys-ProSer-Tyr-Pro-Pro-Thr-Tyr-Lvs. The mussel protein is particularly rich in the amino acid 3,4dihvdroxyphenyl-L-alanine (L-dopa). Catechol oxidase occurs extensively throughout nature and is known to catalyse the ortho hydroxylation of phenols and oxidation of the resulting catechols to o-quinones. Waite proposed, therefore, that catechol oxidase catalyses oxidation of the L-dopa residues in the mussel polyphenolic protein to Lquinone. It was suggested that adhesion results from a combination of coupling of peptidyl-dopa to the bound surface and crosslinking of the polyphenolic protein by reaction of peptidyl-dopa-quinone with nucleophiles such as the E-amino group of lysine res-1dues in the protein.
A catechol oxidase from mushrooms known as mushroom tvrosinase is available commercially and has been shown to hydroxylate tyrosine residues in synthetic decapeptides -'dent'cal in sequence to the repeal sequences in the polyphenclic protein (Marurr.o K. and Waite j.H. (1986) OiDtimization of hvdroxylation of tyrosine and tyrosnecontaining peptides by mushroom tyroslinase. BlochemIca er Bloph_yslca AcLa 872, 98-103).
Large scale production of the mussel polyphenolic protein has been attemiDted commercial adhesive which tyrosinase. Methods for -orotein from mussels are US 4 585 585, and US 4 68 2 z z z with a view to production of a can be crosslinked by mushroom isolation of the polyphenolic described in US 4 496 397, 740. None of these methods, however, have proved to be commercially viable because the polyphenolic protein can on-ly be isolated in small quantities.
'90 97/19141 describes a method of manufacture of an adhesive comprising crosslinking first and second molecules such as gelatin and chitosan, each having one or more aromatic groups, via at least one quinone group. Gelatin and chitosan are _readily available and adhesives formed '--v this method show some resiszance to water. However, the bonds formed are not as strong and durable as those formed by the mussel polyphenolic protein. A further disadvantage that gelatin is not soluble in water at room temperature and has to be heated before use. Ch-'tcsan is only soluble at low nH.
It is desired therefcre to produce bioadhesives which are effective in wet- environments, which can be produced cheaply in bulk quantities, and which have improved,p_roperties over known readily produced bioadhesives.
Extensi- oroteins are hydroxyproline-rich glycoproteins present in the cell walls of dicotyledonous plants. The exact function of extensins is not known, but they have proposed to play a role in the structure of plant walls. Extensins also accumulate in plant cell walls been cell upon 3 wounding and pathogenic attack and are therefore also thought to be involved in defence. It is known that extensins are inherently sticky and their adhesion to glass, polypropylene, and polyearbonate has been described in a papper by Miller' i.G. and Fry, S.C., (1993) (Spinach extensin exhibits characteristics of an adhesive polymer. Acta Bot. ATeerl. 42(2), 221-231). However, the mechanism of adhesion here appears to be a mixture of purely intramolecular forces such as hydrogen bonding and ionic interactions. Oxidative processes are not involved as the adhesion is not inhibited using reducing agents such as ascorbate, mercaptoethanol and dithiothreitol. Althoug'n native non-crosslinked proteins can adhere to inert substances, the set adhesive will be sensitive to moisture. Ultimately strength loss and bond breakage will become apparent. A successful commercial adhesive system must be crosslinked both to improve the strength of the adhesive and to ensure adhesion in wet environments and areas of high moisture.
Extensins have been proposed to form crosslinks by Fry, C.F., (1982) (Isodityrosine, a new crosslinking amino acid f4 rom plant cell wall glycoprotein. Biochem.J. 204, 449-455). Fry suggested that hydrogen peroxide and a peroxidase enzyme such as horseradish peroxidase could be used to form isoditvrosine bonds via an ether linkage between two tyrosine residues. Formation of dityrosine crosslinks via a biphenyl linkage between two tyrosines was not thought to occur. The formation of an isoditvrosine bond and comparison of that linkage with the dityrosine linkage is represented in figure 1 of the accompanying drawings.
The proposed existence of such crosslinking suggests that extensins may form adhesives in the presence of hydrogen peroxide and a peroxidase enzyme. However, it is most unlikely that formation of an adhesive based on addition of a cofactor such as hydrogen peroxide will be practical. Hydrogen peroxide is a relatively low viscosity liquid and would be very difficult to mix with other components of the adhesive which also tend to be relatively viscous. Hydrogen peroxide is also fairly reactive and it 4 . r 0 " 5 2 C 31 1 is likely that bond formation would occur too quickly after it is added to the other components of the adhesive. A further disadvantage of hydrogen peroxide is that it has a r1 Any contamination from, for eatively short shellf-life. example, dirt would introduce bacteria, many of which contain catalase enzv-,nes which breakdown hydrogen peroxide.
Peroxidase has also been proposed to be involved in the hyd-roxylation of L-tyrosine residues to IL-Dopa (K1ibanov A M Berman Z., and Alberti B.N. (1981) Preparative hvdroxvlation of aromatic compounds catalysed by peroxidase. J.Am.Chem.Soc. 103, 6263-6264), suggesting an alternative role for peroxidase in crosslink formation similar to crosslink formation in the mussel polyphenolic protein adhesive. However, this reaction requires oxygen and dihydroxy-fumaric acid and must be carried out at O'C, otherwise non specJLfic oxidation of other amino acids occurs. Use off peroxidase for crosslinking of extensin proteins has therefore not been thought to provide a viable way of producing a commercial adhesive.
It has surprisingly been found that extensin proteins have remarkable adhesive properties.
According to a first aspect of the invention there is provided a co=osition for use as an adhesive comprising:
an extensin Drotein; and e-"ther non-enzymatic bifunctional crosslinking agent; or phenol oxidase and a phenol hydroxylase.
According to a second aspect of the invention there is provided a composition for use as an adhesive comprising:
an extensin protein; -Qhenol oxidase and a phenol hydroxylase; and non-enzymatic bifunctional crosslinking agent.
According to the --'nvent-Jon there is also provided a method for fo----, i-ng an adhesive according to the first aspect of the invention which comiDrises admixing an extensin protein with either:
an amount of a non-enzymat-Lc bifurctional crosslinking agent; or an amount of a phenol oxidase and a phenol hydroxylase effective for inducing crosslinking of the protein.
Z:
Also according to the invention there is provided a method for forming an adhesive according to the second aspect of the invention which comprises admixing an extensin protein. with an amount of a non-enzymatic bifunctional crosslinking agent, a phenol oxidase and a phenol hvdroxvlase effective for inducing crosslinking of the protein.
Each component of compositions according to the invention may be soluble in water.
When using a phenol oxidase and a phenol hydroxylase for crosslinking, it is possible to include as a cofactor a comprises at least one O.L a monohydroxy phenol group or a dihydroxy phenol group. Examples of phenolic moieties which comprise a dihydroxy phenol group include catechol and catechin. The cofactor should be soluble in water. The cofactor may be present at about 1% weight by volume of the composition.
The term "extensin protein" used herein is defined for the purposes of this application as covering:
(i) natural extensin proteins, such as plant extensins (for example carrot, spinach, etc.); (ii) non-natural synthetic extens-ins, such as extensins produced chemically or by expression of _recombinant DNA JLn a suitable host; (iii) extensin derivatives (whether chemical or synthetic) which have amino acid sequences which differ from the extensin sequences by virtue of amino acid substitution, deletion, or addition, protease truncation or post translational modification; but which retain extensin activity.
Natural extensin protein as referred to in (i) above is a plant protein rich in hydroxyproline, tyrosine and lvs--'ne residues. The content of hydroxyproline in carrot extensin is at least 50%, the content of tyrosine is at least 10.1%, and the content of lysine is at least 6.9%.
DNA encoding carrot extensin has been cloned (Chen J. and Va-rner J.E. (1985) An extracellular matrix protein in plants: characterisation of a genomic clone for carrot extensin. EMBO J. 4, 2145-2151; Chen J. and Varner JE (1985) chenolic moietv whic Isolation and characterisation of cDNA clones for carrot extensin and a proline-_rich 33KDa protein.
Proc.v'a'1.Acad.Sc--L'.USA 82, 4399-4403).
c:
0 2 C 3 = Derivatives of the extensin as referred to in (--lii) above mav be obtained by ex-p-ression. of a modified DNA including a modified extensin gene. A derivative of the extensin may be substantially free of carbohydrate.
The extensin protein may be present in the composition in ar amount upto about 50% weight by volume of the composition, for example, the ex-ens-J., i protein may be present in the composition in an amount from about 20% to about 30% weight by volume of the composition.
A procedure for isolation of an extensin according to the invention from carrots is described below:
Carrot extensin proteins were isolated from cores (7rrir,) of phloem parenchyma sliced with a scalpel into lmm thick slices. Carrot preparations (90g) (finely chopped or gently homogenised', were washed twice in distilled water and incubated in pozassium phosphate buffer (5mM, pH 6.0) containing chloramphenicol (50mg/m1) -for three days at 2CC with s'-akinc. The extraction buffer was exchanged each day. On completion, the carrots were washed in distilled water and immersed in a solution (600mi) containing polyvinyl polypyrro'Lidone (PVF1-P) (9g) and dithiothreitol (DT1) (-"rnV-, -final concentration', The tissue was homogenised for two minutes in a blender, pelleted by centrifugation and washed with eight litres of distilled water. The cell wall pellet was further extracted (3 times) with 20OmI of a solution containing calcium chloride (0.2M final concentration), DTT final concentra.ion', and:-VIPP (9g) On centrifugatlon the sunerna,ants were pooled, filtered to remove anv sol-- material and reduced to a volume of SOM1 us i na u--"tra-f-i-'trat--'on (10,0C0 molecular weight cut-off) Tr, e concentraied extract was dialysed overnight in distilled water at 4,-- and further reduced in volume to 10m_ bv ul.:ira'ilt--a--ion. Each 1OmI volume was adjusted with IM (p.H 8) to give a final 7r-"s concentration of The material was then applied to a cation exchange column (12 x 1.5 cm) (CM-Sepharose CL-6B) previously equilibrated with tr-is/HCl (1OMM, pH 8) and the protein fractions eluted using one column volume of tris/HCl (pH 8) followed by a linear gradient (60m1) of 10-30OmM tris/HC! (pH 8). T_ he elution profile was monitored at 280= and the frac--io.-s (3m1) corres.;:)onding to each peak were pooled and dialysed overnight with sodium acetate (10OmM, PH 6) at 40C. The dialysed samples were freeze-dried and weighed before further analysis. In all purifil cations peak 1 from the cation exchange column was ignored as it was primarily made uO of PvPP.
It is noted herein that peroxidases are not phenol oxidases. Peroxidases act by hydrolysing hydrogen peroxide. it is possible that oxygen liberated by this reaction can oxidise phenolics, but this oxidation does not occur by an enzymatic process. Phenol oxidation is not possible in the presence of a peroxidase without the addition of hydrogen -ceroxide. It is also noted herein that peroxidases are not phenol hydroxylases.
The phenol oxidase and the phenol hydroxylase may be a tyrosinase. The composition can contain at least 0.005% weight by volume of tyrosinase. Tyrosinase has the advantage that it is readily available from a variety of sources. The tyrosinase may be a mushroom tyrosinase. The mushroom tyrosinase may be Agaricus bisporus tyrosinase.
The non-enzymatic bifunctional crosslinking agent may be p_resent in the composition from about 0.1% to about 5% weight by volume of the composition. The non-enzymatic bifunctional crosslinking agent may be any non-enzymatic bifunctional crosslinking agent capable of inducing crosslinking of a composition for use as an adhesive according to the invention. The non-enzymatic bifunctional crosslinking agent may be at least one of glutaraldehyde, a di-isocyanate, or a quinone. The diisocyanate may be Trixene, for example Trixene BI 7986 (Baxenden). Trixene has the advantage that it is blocked and unreactive until the temoerature reaches 130C. Compositions according to the invention that comprise Trixene may therefore form a thermosetting adhesive. The quinone may be a benzoquinone or a derivative thereof. The amount of the benzoquinone in the composition can be about 1% weight by volume of the composition. The benzoquinone may be 1,2-benzoquinone, 1,3- benzoquinone, or 1,4-benzoeruinone.
It has been found that the rate of oxidation of groups mav be conveniantly controlled by varying the amount of phenol oxidase and phenol hydroxylase that is added, allowing the rate of linkace o be readily controlled. The rate of linkage may also be controlled by varying the amount of the non-enzvmatic bifunctional cross!-"nking agent.
When compositions according to the invention that contain the nonenzvmatic bifunctional crosslinking agent form crosslinks, the nonenzymatic bifunczional crosslinking agent reacts with the E-amino group of lys--'ne residues the extensin protein. Each molecule of non-enzYmatic bifunctional crosslinking agent can react with upto two i5 lysine res--'dues. When the two lysine residues are in different protein molecules, crosslinks are formed between different protein molecules. When the two lysine residues crosslinks are formed are in the same protein molecule, within the same protein molecule.
When compositions according to the invention that comprise the phenol oxidase and the phenol hydroxylase form crosslinks, the phenol hydroxylase catalyses th e hydroxylation of the phenol group of tyrosine residues in the protein -7-o form a d--'hydroxv phenol group and the phenol oxidase catalyses the oxidation of the dihydroxy phenol group to form a quinone group. The quinene group of the modified tvros-ine residue may then react with the E-amino group of two lysine residues in the protein. When one or bo-:ih of the lysine residues are in the same protein molecule as the modified tvrosine residue containing the quinone group, intramolecular crosslinking occurs. When one or both of the lysine residues are in different protein molecules to the modified tyrosine residue containing the quinone group, intermolecular crosslinking occurs.
Tvrosinase has the advantage that- it is a phenol hydroxylase and a phenol oxidase. It will be appreciated therefore that compositions according to the invention which comprise tyrosinase have the advantage that a separate phenol oxidase and a phenol hydroxylase do not have to be 32 3:
i 0 -,5 2 5 added to the composition because the phenol oxidase and the phenol hydroxylase activity are on a single molecule.
The hydroxylation and oxidation of a tyrosine residue by tyrosinase is shown in figure 2 of the accompanying drawings. Figure 2 also shows reaction of the oxidised tyros.ine residue with the e-amino group of a lysine residue in the same protein molecule.
When compositions according to the invention that comprise the phenol oxidase and the phenol hydroxylase further include a cofactor which comprises a phenolic moiety with a monohydroxy phenol group, the phenol hydroxylase catalyses the hydroxylation of the monohydroxy phenol group in the cofactor to form a dihydroxy phenol group and the phenol oxidase catalyses the oxidation of the dihydroxy phenol group to form a quinone group. The quinone group of the modified cofactor may then react with the E-amino group of lysine residues in the protein to form crossl--'nks within the same protein molecule or between different protein molecules.
when compositions according to the invention that comprise the phenol oxidase and the phenol hydroxylase further include a cofactor which comprises a phenolic moiety with a dihydroxy phenol group, the phenol oxidase catalyses the oxidation of the dihydroxy phenol group of the cofactor to form a quinone group. The quinone group of the modified cofactor mav then react with the E-amino group of!vs-,'ne residues in the protein to form crosslinks within the same protein molecule or between different protein molecules. Thus, a cofactor comprising a monohydroxy phenol group or a dihydroxy phenol group may be used to increase the number of crosslinks formed compared to compositions according to the invention which comprise the phenol oxidase and the phenol hydroxylase that do not include the cofacto-r. The number of crosslinks which can potentially be formed may also be increased by increasing the number of tyrosine and/or lysine residues in the extensin protein by recombinant means. However, care should be taken not to increase the number of crosslinks formed too much as over-crosslinked adhesives can be brittle.
- - 0 - , C 4 J. - compositions according to It will be appreciated tha the invention t'.,iat comprise a cofactor which includes a d-ihvdroxy phenol group may form crosslinks in the absence of the phenol hydroxylase. there is also provided according -.c the invention a Composition for use as an adhesive which comprises:
an extensin protein; co.Eactor comerising a dihydroxy phenol group; phenol oxidase; and optionally non-enzymatic bifunctional crosslinking agent.
There is also provided a method for forming an adhesive which comprises admixing an extensin protein with an amount of a cofactor comprising a dihydroxy phenol group, a phenol oxidase, and optionally a non-enzymatic bifunctional crosslinking agent effective for inducing crosslink--'ng of the prote-^n.
According to the invention there is also provided a kit for manufacture of an adhesive, the kit comprising separate componen-.s, where-in admixture of the separate components forms a --omposition according to the invention.
to the invention there is also provided a kit for manufacture of an adhesive that comprises separate first and second comconents, the first component comprising an extensi- --'-e second component comprising: either non-enzymatic bifunctional crosslink'.ng agent; or P'-enol oxidase and a phenol hyd-roxylase and optionally a cofator; wherein admixture of the first and second comoonents forms a compositlon according to the invent'Lon.
Also according to the invention there is provided a kit for manufacture of an adhesive that comprises separate and second comiDonents, the first com-Qonent comprising an extensin nrotein, the second component comprising a none7.zvrr.atic bifunctional cross-' inking agent and a phenol oxidase and a phenol hydroxylase and optionally a cofactor, wherein admixture of the first and second components forms a composition according to the invention.
Adhesives formed using compositions according to the invention have excellent strength, durability and water resistant propert Les. They are readily produced in bulk 11 - 13 2 0 3 0 quantities and at low cost. The strength of adhesives according to the invention has been found to be at least as good as the strength of conventional water resistant adhesives.
Adhesives according to the invention have been found to have several uses. Adhesives according to the invention may adhere to water-absorbent substrates and can be used to adhere such substrates together. Adhesives of the present invention may adhere to a substrate having a hydroxy aromatic, dihydroxy aromatic, hydroxy phenone or amino group and can be used to adhere such substrates together. For example the substrate may be wood, leather, cotton, paper, carpet, or a textile.
Adhesives according to the invention have also beer. found to adhere to non water-absorbent substrates and can be used to adhere non waterabsorbent substrates to each other or to water absorbent substrates. For example, the non water-absorbent substrate may be a metal or a plastic.
Adhesives according to the invention may be used to bind together particulates. Examples of particulates include sand and glass fibre.
Adhesives according to the invention may be used as an undercoat to a protective coating such as a paint or to a coating such as a non waterresistant adhesive. Undercoats comprising adhesives according to the invention have been found to have the advantage that the coating that is subsequently applied to the undercoat is significantly more resistant to the effects of water than coatings applied in the absence of the undercoat or to coatings applied to a conventional undercoat.
Adhesives according to the invention may be used as a suture to close wounds. Sutures formed according to the invention have the advantage that they are resistant to water and may have reduced antigenicity compared to conventional sutures.
Adhesives according to the invention may be used as a gelling agent in food products.
According to the invention there is also provided a oharmaceutical composition comprising a pharmaceutically - 12 active ingredient and a crosslinked adhesive composition according to the invention.
13 -
Claims (1)
- Claims -10 1. A composition for use as an adhesive comprising: an extensinprotein; and either non-enzymatic bifunctional crosslinking agent; or zhenol oxidase and a phenol hydroxylase.A composition for use as an adhesive comprIsing: an extensin protein; non-enzymatic bifunctional crosslinking agent; and phenol oxidase and a phenol hyd-roxylase.3. A composition according to claim, 1 or 2 which further comprises a cofactor when the composition comprises a phenol oxidase and a phenol hydroxylase.4. A method for forming an adhesive which comprises admixing an extensin protein with either: an amount of a non-enzymatic bifunctional crosslinking agent; or an amount of a phenol oxidase and a phenol hydroxylase effective for inducing crosslinking of the protein.r, A method for forming an adhesive which comcrJses admixing an extensin protein with an amount of a nonenzymatic bifunctional crosslinking agent, a phenol oxidase and a phenol hydroxylase effective for inducing crosslinking of the protein.6. A method for forming an adhesive which compr'ses admixing an extensin protein either with an amount of a cofactor, a phenol oxidase and a phenol hydroxylase effective for inducing crosslinking of the protein or wit'an amount of a cofactor, a non-enzymatic bifunctional crosslinking agentY a phenol oxidase and a phenol hydroxylase effective for inducing crosslinking of the protein.- - 4 - 7. A composition or method according to claim 3 or 6 in which the cofactor comprises a phenolic mo-ietv which c=rises at least one of a monohydroxy phenol group or a dihvdroxy phenol group.8. A composition or me 1 thod ac cording to claim 3, 6, or 7 in which the cofactor is soluble in water.9. A composition or method according to claim 7 or 8 in which the cofactor comprises catechin.c 10. P% comcosition or method according to any of claims 7 to 9 in which the cofactor comprises catechol.-, 1. A comcosition or method according -to any p-receding claim in which the ncn-enzymat--',c bifunctional crosslinking agent comprises glutaraldehyde.12. A co=osition or method according to any preceding cl-aim in which the non-enzymat-Lc bifunctional crosslinking agent comprises a di-isocyanate.1-3. A composition or method according to claim 12 in which the diisocvanate is Trixene.14. A composition or method accord-ing to any preceding claim in which the non-enzvmatic b-'fun-zional crosslinking agent comprIses a au--none.15. A comcosi-Lion or method accord-'ng to claim 14 in which the auinone is a benzoquinone.z composition or method according to any preceding c'aim in which the tD'enol' oxidase and the phenol 'hydroxylase is a tvrosinase.-7. A composition or method according to claim 16 in which L the tyrosinase is a mushroom tyrosinase.- 18. A composition or method according to claim 17 in which the mushroom tyrosinase is Agaricus bisporus tyrosinase.19. Use of a composition or method according to any preceding claim for binding substrates together.z 20. Use according to claim 19 in which the substrates are non waterabsorbent 21. Use according to claim 19 in which the substrates are water absorbent.22. Use according to claim 19 in which the substrates comprise a non water-absorbent substrate and a water absorbent substrate.23. Use according to claim 20 or 22 in which the non waterabsorbent substrate or substrates comprise at least one of metal or plastic.24. Use according to claim 21 or 22 in which the water absorbent substrate or substrates comprise at least one of wood, leather, cotton, paper, carpet, or textile.25. Use according to claim 19 as a binder of particulates.26. Use according to claim 25 in which the particulates com-orise at least one of sand or glass fibre.27. Use according to claim 19 as an undercoat to a coazing.28. Use according to claim 27 in which the coating is a,:)ain-L.29. Use according to claim 27 in which the coating is an adhesive.Use according to claim 19 as a sutu--e for closing a wound.- 16 31. Use according to claim 30 in a method for closing a wound.32. Use according to claim 19 as a gelling agent in foo,-i products.33. A pharmaceutical comcosition comprising a )r.a--maceutically active ingred'jent and a crosslinked adhesive composition according to any of claims 1 to 3 or to 18.0 2 3 Cl 34. A k i for manufacture of an adhesive, the ki-comprising separate components, whe-rein admixture of the separate components forms an adhesive composition according to anv of claims 1 to 3 or 7 to 18.35. A kit for manufacture of an adhesive that comprises separate first and second components, the first componen- comprising an extensin protein, tle second comoonent comDri-,,:zing: either r.on-enz-,matic bifunctional crosslinking agent; or chenol oxidase and a phenol hydroxylase and opt.-Lona-',lv a cofator; wherein admixture of the first and second components forms a composition according to any of claims 1 to 3 or 7 to 18.36. A kit for manufacture of an adhesive that comprises seDarate first and second components, the first componen-comprising an extensin protein, the second component comprising a non-enzymatic bifunctional crosslinking agent and a oheno-' oxidase and a phenol hyd-roxv-'ase and optionally a cofactor, wherein admixture of the first and second co=onents forms a composition according to any of claims 1 to 3 or 7 to 18.-ion for use as an adhesive substantially as comoosit described with reference to figure 2 of the accompanying drawings.38. A method for forming an adhesive substantially as described with reference to figure 2 of the accompanying drawings.39. A kit for manufacture of an adhesive substantially as described with reference to figure 2 of the accompanying drawings.
Priority Applications (7)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| GB9807777A GB2336156B (en) | 1998-04-09 | 1998-04-09 | Adhesives |
| DE69902903T DE69902903T2 (en) | 1998-04-09 | 1999-04-08 | ADHESIVES |
| EP99915887A EP1080158B1 (en) | 1998-04-09 | 1999-04-08 | Adhesives |
| AU34311/99A AU754998B2 (en) | 1998-04-09 | 1999-04-08 | Adhesives |
| CA002327109A CA2327109A1 (en) | 1998-04-09 | 1999-04-08 | Adhesives |
| PCT/GB1999/001080 WO1999052988A1 (en) | 1998-04-09 | 1999-04-08 | Adhesives |
| AT99915887T ATE223949T1 (en) | 1998-04-09 | 1999-04-08 | ADHESIVES |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
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| GB9807777A GB2336156B (en) | 1998-04-09 | 1998-04-09 | Adhesives |
Publications (3)
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| GB9807777D0 GB9807777D0 (en) | 1998-06-10 |
| GB2336156A true GB2336156A (en) | 1999-10-13 |
| GB2336156B GB2336156B (en) | 2003-05-07 |
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ID=10830227
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|---|---|---|---|
| GB9807777A Expired - Fee Related GB2336156B (en) | 1998-04-09 | 1998-04-09 | Adhesives |
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| EP (1) | EP1080158B1 (en) |
| AT (1) | ATE223949T1 (en) |
| AU (1) | AU754998B2 (en) |
| CA (1) | CA2327109A1 (en) |
| DE (1) | DE69902903T2 (en) |
| GB (1) | GB2336156B (en) |
| WO (1) | WO1999052988A1 (en) |
Cited By (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2007090384A2 (en) * | 2006-02-09 | 2007-08-16 | Ernst-Moritz-Arndt-Universität Greifswald | Adhesives and adhesive methods |
| WO2009060439A2 (en) * | 2007-11-05 | 2009-05-14 | Technion - Research & Development Foundation Ltd | Adhesives and methods of applying the same |
| CN101955748A (en) * | 2010-11-04 | 2011-01-26 | 漳州市圣木林业科技有限公司 | Formaldehyde-free corn protein powder wood adhesive and preparation method thereof |
| US8791219B2 (en) | 2012-03-23 | 2014-07-29 | California Institute Of Technology | Rapidly crosslinkable adhesives for biomedical applications |
| US9216234B2 (en) | 2009-06-01 | 2015-12-22 | Technion Research & Development Foundation Ltd. | Sealants, manufacturing thereof, and application thereof |
| CN106318313A (en) * | 2016-09-28 | 2017-01-11 | 书香门地(上海)新材料科技有限公司 | Formaldehyde-free soybean-protein-based adhesive for multilayer solid-wood composite floorboard and preparation method of formaldehyde-free soybean-protein-based adhesive |
Families Citing this family (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE102007045066A1 (en) * | 2007-09-20 | 2009-04-02 | Mike Ehrlich | Hemostatic material containing synthetic peptides or polysaccharides |
| KR101257996B1 (en) * | 2010-11-01 | 2013-04-30 | 아주대학교산학협력단 | Immobilization method of bioactive molecules using polyphenoloxidase |
| RU2753338C2 (en) | 2017-05-11 | 2021-08-13 | Роквул Интернэшнл А/С | Fire-fighting insulation product and application of such product |
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| US5202256A (en) * | 1984-09-13 | 1993-04-13 | Enzon Labs, Inc. | Bioadhesive precursor protein expression vectors |
| ATE68813T1 (en) * | 1986-04-25 | 1991-11-15 | Bio Polymers Inc | ADHESIVE DERIVATIVES OF BIOADHAESIVE POLYPHENOLPROTEINS. |
| JPH04334396A (en) * | 1991-05-09 | 1992-11-20 | Hitachi Chem Co Ltd | Insolubilizing protein containing lysine and tyrosine and insolubilized protein |
| JP2688559B2 (en) * | 1992-06-30 | 1997-12-10 | 日本ビー・エックス・アイ株式会社 | Composition for adhering biological tissue |
| IT1271342B (en) * | 1994-12-28 | 1997-05-27 | Indena Spa | PROTEINS RICH IN HYDROXYPROLIN AND PHARMACEUTICAL AND COSMETIC FORMULATIONS CONTAINING THEM |
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- 1998-04-09 GB GB9807777A patent/GB2336156B/en not_active Expired - Fee Related
-
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- 1999-04-08 EP EP99915887A patent/EP1080158B1/en not_active Expired - Lifetime
- 1999-04-08 AT AT99915887T patent/ATE223949T1/en not_active IP Right Cessation
- 1999-04-08 AU AU34311/99A patent/AU754998B2/en not_active Ceased
- 1999-04-08 DE DE69902903T patent/DE69902903T2/en not_active Expired - Fee Related
- 1999-04-08 CA CA002327109A patent/CA2327109A1/en not_active Abandoned
- 1999-04-08 WO PCT/GB1999/001080 patent/WO1999052988A1/en active IP Right Grant
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| US5443855A (en) * | 1991-09-18 | 1995-08-22 | Revlon Consumer Products Corporation | Cosmetics and pharmaceuticals containing extensins and related methods |
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Cited By (14)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2007090384A2 (en) * | 2006-02-09 | 2007-08-16 | Ernst-Moritz-Arndt-Universität Greifswald | Adhesives and adhesive methods |
| WO2007090384A3 (en) * | 2006-02-09 | 2008-09-12 | Univ Ernst Moritz Arndt | Adhesives and adhesive methods |
| US8440209B2 (en) | 2006-02-09 | 2013-05-14 | Stryker Trauma Gmbh | Adhesive for medical applications and means for haemostasis |
| US20110015125A1 (en) * | 2007-11-05 | 2011-01-20 | Technion-Research & Development Foundation Ltd | Adhesives and methods of applying the same |
| WO2009060439A3 (en) * | 2007-11-05 | 2010-04-01 | Technion - Research & Development Foundation Ltd | Adhesives and methods of applying the same |
| WO2009060438A3 (en) * | 2007-11-05 | 2010-04-01 | Technion - Research & Development Foundation Ltd | Adhering bandage and methods of applying the same |
| WO2009060438A2 (en) * | 2007-11-05 | 2009-05-14 | Technion - Research & Development Foundation Ltd | Adhering bandage and methods of applying the same |
| WO2009060439A2 (en) * | 2007-11-05 | 2009-05-14 | Technion - Research & Development Foundation Ltd | Adhesives and methods of applying the same |
| US8673354B2 (en) * | 2007-11-05 | 2014-03-18 | Technion Research And Development Foundation Ltd. | Adhesives and methods of applying the same |
| US8709480B2 (en) | 2007-11-05 | 2014-04-29 | Technion Research And Development Foundation Ltd. | Adhering composition and method of applying the same |
| US9216234B2 (en) | 2009-06-01 | 2015-12-22 | Technion Research & Development Foundation Ltd. | Sealants, manufacturing thereof, and application thereof |
| CN101955748A (en) * | 2010-11-04 | 2011-01-26 | 漳州市圣木林业科技有限公司 | Formaldehyde-free corn protein powder wood adhesive and preparation method thereof |
| US8791219B2 (en) | 2012-03-23 | 2014-07-29 | California Institute Of Technology | Rapidly crosslinkable adhesives for biomedical applications |
| CN106318313A (en) * | 2016-09-28 | 2017-01-11 | 书香门地(上海)新材料科技有限公司 | Formaldehyde-free soybean-protein-based adhesive for multilayer solid-wood composite floorboard and preparation method of formaldehyde-free soybean-protein-based adhesive |
Also Published As
| Publication number | Publication date |
|---|---|
| DE69902903D1 (en) | 2002-10-17 |
| ATE223949T1 (en) | 2002-09-15 |
| AU3431199A (en) | 1999-11-01 |
| CA2327109A1 (en) | 1999-10-21 |
| GB9807777D0 (en) | 1998-06-10 |
| GB2336156B (en) | 2003-05-07 |
| AU754998B2 (en) | 2002-11-28 |
| WO1999052988A1 (en) | 1999-10-21 |
| EP1080158A1 (en) | 2001-03-07 |
| EP1080158B1 (en) | 2002-09-11 |
| DE69902903T2 (en) | 2003-08-28 |
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| PCNP | Patent ceased through non-payment of renewal fee |
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